Research workbench

T4 lysozyme mutant C54T/C97A/L121A/L133A in the presence of 8 atm xenon

Analyse T4 lysozyme mutant C54T/C97A/L121A/L133A in the presence of 8 atm xenon in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1C68
Type: protein
Length: 162 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein (lysozyme)
EC: 3.2.1.17
UniProt: P00720
Ligands: XE, CL
Pockets: 1 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 64% helix, 9% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein (lysozyme) (EC 3.2.1.17)	protein	162	64% helix, 9% strand	P00720

Ligands and binding sites

XE · Xenon · ion · 3 copies · chains A
CL · Chloride ion · ion · 2 copies · chains A
BME · Beta-mercaptoethanol · additive · 2 copies · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	275	0.52	0.75	31	empty

Compared structures

1C68 · T4 lysozyme mutant C54T/C97A/L121A/L133A in the presence of 8 atm xenon · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P00720
Elsewhere: RCSB PDB 1C68 · PDBe 1C68 · UniProt P00720

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